SH3 domains are structurally well-characterized as monomeric modular units of protein structure that mediate protein-protein recognition in numerous signal transduction proteins. The X-ray crystallographic structure of the Eps8 SH3 domain reveals a novel variation of the canonical SH3 fold: the SH3 domain from Eps8 is a dimer formed by strand interchange. In addition, co-immunoprecipitation experiments show that intact Eps8 is multimeric in vivo. Hence, the SH3 domain of Eps8 may represent a dimerization motif.
The SH3 domain of Eps8 exists as a novel intertwined dimer / K. V. Kishan, G. Scita, W. T. Wong, P. P. Di Fiore, M. E. Newcomer. - In: NATURE STRUCTURAL BIOLOGY. - ISSN 1072-8368. - 4:9(1997 Sep), pp. 739-43-743.
The SH3 domain of Eps8 exists as a novel intertwined dimer
G. ScitaSecondo
;P. P. Di FiorePenultimo
;
1997
Abstract
SH3 domains are structurally well-characterized as monomeric modular units of protein structure that mediate protein-protein recognition in numerous signal transduction proteins. The X-ray crystallographic structure of the Eps8 SH3 domain reveals a novel variation of the canonical SH3 fold: the SH3 domain from Eps8 is a dimer formed by strand interchange. In addition, co-immunoprecipitation experiments show that intact Eps8 is multimeric in vivo. Hence, the SH3 domain of Eps8 may represent a dimerization motif.
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